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DC Field | Value | Language |
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dc.citation.endPage | 19702 | - |
dc.citation.number | 22 | - |
dc.citation.startPage | 19697 | - |
dc.citation.title | JOURNAL OF BIOLOGICAL CHEMISTRY | - |
dc.citation.volume | 277 | - |
dc.contributor.author | Chang, JS | - |
dc.contributor.author | Seok, H | - |
dc.contributor.author | Kwon, TK | - |
dc.contributor.author | Min, DS | - |
dc.contributor.author | Ahn, BH | - |
dc.contributor.author | Lee, YH | - |
dc.contributor.author | Suh, JW | - |
dc.contributor.author | Kim, JW | - |
dc.contributor.author | Iwashita, S | - |
dc.contributor.author | Omori, A | - |
dc.contributor.author | Ichinose, S | - |
dc.contributor.author | Numata, O | - |
dc.contributor.author | Seo, Jeong Kon | - |
dc.contributor.author | Oh, YS | - |
dc.contributor.author | Suh, Pann-Ghill | - |
dc.date.accessioned | 2023-12-22T11:38:27Z | - |
dc.date.available | 2023-12-22T11:38:27Z | - |
dc.date.created | 2014-09-02 | - |
dc.date.issued | 2002-05 | - |
dc.description.abstract | The pleckstrin homology (PH) domain is a small motif for membrane targeting in the signaling molecules. Phospholipase C (PLC)-γ1 has two putative PH domains, an NH2-terminal and a split PH domain. Here we report studies on the interaction of the PH domain of PLC-γ1 with translational elongation factor (EF)-1α, which has been shown to be a phosphatidylinositol 4-kinase activator. By pull-down of cell extract with the glutathione S-transferase (GST) fusion proteins with various domains of PLC-γ1 followed by peptide sequence analysis, we identified EF-1α as a binding partner of a split PH domain of PLC-γ1. Analysis by site-directed mutagenesis of the PH domain revealed that the β2-sheet of a split PH domain is critical for the interaction with EF-1α. Moreover, Dot-blot assay shows that a split PH domain specifically binds to phosphoinositides including phosphatidylinositol 4-phosphate and phosphatidylinositol 4, 5-bisphosphate (PIP2). So the PH domain of PLC-γ1 binds to both EF-1α and PlP2. The binding affinity of EF-1α to the GST·PH domain fusion protein increased in the presence of PIP2, although PIP2 does not bind to EF-1α directly. This suggests that EF-1α may control the binding affinity between the PH domain and PIP2. PLC-γ1 is substantially activated in the presence of EF-1α with a bell-shaped curve in relation to the molar ratio between them, whereas a double point mutant PLC-γ1 (Y509A/F510A) that lost its binding affinity to EF-1α shows basal level activity. Taken together, our data show that EF-1α plays a direct role in phosphoinositide metabolism of cellular signaling by regulating PLC-γ1 activity via a split PH domain. | - |
dc.identifier.bibliographicCitation | JOURNAL OF BIOLOGICAL CHEMISTRY, v.277, no.22, pp.19697 - 19702 | - |
dc.identifier.doi | 10.1074/jbc.M111206200 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.scopusid | 2-s2.0-0037205420 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/5689 | - |
dc.identifier.url | http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0037205420 | - |
dc.identifier.wosid | 000175894800061 | - |
dc.language | 영어 | - |
dc.publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | - |
dc.title | Interaction of elongation factor-1 alpha and pleckstrin homology domain of phospholipase C-gamma 1 with activating its activity | - |
dc.type | Article | - |
dc.description.journalRegisteredClass | scopus | - |
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